Analytical Data
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基因名
RFP2
- Application
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别名
TRIM13; LEU5; RFP2; RNF77; E3 ubiquitin-protein ligase TRIM13; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Leukemia-associated protein 5; Putative tumor suppressor RFP2; RING finger protein 77; RING-type E3 ubiquitin transferase TRIM13; Ret finger protein 2; Tripartite motif-containing protein 13
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O60858
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表达区间
1-410 aa
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氨基酸序列
MDVMELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLLILLLGLVIVFGPTMFLEWSLFDDLATWKGCLSNFSSYLTKTADFIEQSVFYWEQVTDGFFIFNERFKNFTLVVLNNVAEFVCKYKLL
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分子量
73.7 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
RFP2, a member of the ring finger protein family, plays a crucial role in various cellular processes, including DNA repair, cell cycle regulation, and protein degradation. Its unique structural features, characterized by a RING-finger domain, allow it to function as an E3 ubiquitin ligase, facilitating the transfer of ubiquitin molecules to target proteins. This post-translational modification is essential for proteasomal degradation and the modulation of protein activity, ultimately influencing numerous signaling pathways. Research on RFP2 has gained momentum due to its implications in cancer biology, where aberrant expression or mutations can lead to disrupted cellular homeostasis and tumorigenesis. Furthermore, the interaction of RFP2 with other cellular partners suggests its involvement in complex regulatory networks. Understanding the molecular mechanisms underlying RFP2 functionality not only sheds light on its physiological roles but also opens avenues for therapeutic interventions, particularly in cancer. The exploration of RFP2 as a potential biomarker or target for novel drugs is crucial in the development of strategies to combat malignancies linked to its dysregulation. As such, the study of RFP2 and its recombinant protein form is pivotal in elucidating the intricate balance of cellular processes and addressing challenges in targeted cancer therapies.
